SitesBLAST

5xoqA Crystal structure of o-acetylserine sulfhydrylase with bound transcription factor peptide inhibitor from planctomyces limnophilus
46% identity, 97% coverage: 11:318/318 of query aligns to 10:307/310 of 5xoqA

query
sites
5xoqA

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binding : T72 (= T73), S73 (= S74), G74 (= G75), T76 (= T77), M123 (≠ G124), Q144 (= Q155), R218 (≠ K230), H219 (= H231), Q222 (= Q234), G223 (= G235), A226 (≠ Y238)

P9WP55 O-acetylserine sulfhydrylase; OAS sulfhydrylase; OASS; Cysteine synthase A; CSase A; O-acetylserine (thiol)-lyase A; OAS-TL A; O-acetylserine-specific cysteine synthase; Sulfide-dependent cysteine synthase; EC 2.5.1.47 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
43% identity, 98% coverage: 6:317/318 of query aligns to 4:305/310 of P9WP55

query
sites
P9WP55

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K44 (= K46) modified: N6-(pyridoxal phosphate)lysine
N74 (= N76) binding pyridoxal 5'-phosphate
GTGGT 178:182 (≠ GTSGT 189:193) binding pyridoxal 5'-phosphate
S266 (≠ T279) binding pyridoxal 5'-phosphate

2q3dA 2.2 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) from mycobacterium tuberculosis in complex with the reaction intermediate alpha-aminoacrylate (see paper)
43% identity, 98% coverage: 6:317/318 of query aligns to 4:305/306 of 2q3dA

query
sites
2q3dA

C

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F

active site: K44 (= K46), S266 (≠ T279), P293 (≠ C305)
binding 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-propionic acid: K44 (= K46), T71 (= T73), S72 (= S74), N74 (= N76), T75 (= T77), Q144 (= Q155), V177 (= V188), G178 (= G189), T179 (= T190), G180 (≠ S191), T182 (= T193), G222 (= G235), I223 (≠ S236), S266 (≠ T279), P293 (≠ C305), D294 (= D306)

2efyA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-acetylbutyric acid
44% identity, 96% coverage: 12:317/318 of query aligns to 6:301/302 of 2efyA

query
sites
2efyA

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A

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F

Y

active site: K40 (= K46), S70 (= S74), E200 (= E214), S204 (≠ A218), S263 (≠ T279)
binding 5-oxohexanoic acid: T69 (= T73), G71 (= G75), T73 (= T77), Q141 (= Q155), G175 (= G189), G219 (= G235), M220 (≠ S236), P222 (≠ Y238)
binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ D186), G175 (= G189), T176 (= T190), G177 (≠ S191), T179 (= T193), G219 (= G235), S263 (≠ T279), P289 (≠ C305), D290 (= D306)

2ecqA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 3-hydroxylactate
44% identity, 96% coverage: 12:317/318 of query aligns to 6:301/302 of 2ecqA

query
sites
2ecqA

A

A

I

I

G

G

H

K

T

T

P

P

L

V

I

V

E

R

L

L

G

A

R

K

V

V

G

V

R

E

D

P

L

D

P

M

A

A

R

E

I

V

W

W

A

V

K

K

A

L

E

E

F

G

M

L

N

N

P

P

G

G

S

S

M

I

K
|
K

D

D

R

R

I

P

A

A

L

W

K

Y

M

M

I

I

E

K

D

D

A

A

E

E

Q

E

A

R

G

G

K

I

L

L

K

R

P

P

G

G

-

S

-

G

D

Q

T

V

V

I

L

V

E

E

E

P

T

T

S
|
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

M

M

V

I

C

A

A

A

I

S

K

R

G

G

Y

Y

P

R

F

L

I

I

A

L

V

T

M

M

S

P

E

A

G

Q

N

M

S

S

P

E

E

E

R

R

R

K

Q

R

I

V

L

L

K

K

A

A

L

F

G

G

A

A

K

E

V

L

E

V

L

L

V

T

-

D

P

P

Q

E

A

R

E

R

G

-

K

-

P

-

G

-

Q

-

V

-

T

-

G

-

D

-

L

M

A

L

L

A

V

A

E

R

K

E

R

E

A

A

G

L

E

R

L

L

Q

K

Q

E

E

E

L

L

G

G

A

A

F

F

W

M

V

P

N

D

Q
|
Q

F

F

H

K

N

N

P

P

S

A

N

N

C

V

A

R

G

A

H

H

Y

Y

E

E

T

T

A

G

Q

P

E

E

I

L

W

Y

E

E

Q

A

M

L

E

E

G

G

R

R

I

I

D

D

Y

A

F

F

V

V

D
x
Y

V
x
G

V

S

G
|
G

T
|
T

S

G

G

G

T
|
T

F

I

T

T

G

G

I

V

A

G

T

R

A

Y

L

L

K

K

E

E

K

R

D

I

P

P

K

H

I

V

Q

K

C

V

W

I

V

A

V

V

E
|
E

P

P

A

A

S

R

A
x
S

P

N

V

V

L

L

A

S

G

G

K

G

P

K

V

M

T

G

N

-

P

-

K

Q

H

H

V

G

L

F

Q

Q

G
|
G

S

M

S

G

Y

P

A

G

K

F

I

I

P

P

A

E

L

N

W

L

K

D

P

L

E

S

V

L

C

L

D

D

G

G

Y

V

I

I

T

Q

V

V

T

W

D

E

G

E

E

D

A

A

I

F

R

P

T

L

S

A

R

R

L

L

A

A

S

R

E

E

G

G

L

L

L

F

V

L

G

G

Y

M

T
x
S

A

S

G

G

N

I

V

V

A

W

A

A

L

L

R

Q

M

V

A

A

G

R

W

E

C

L

D

G

P

P

G

G

A

K

N

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D

D

S

G

G

G

M

W

K

K

Y

Y

L

L

S

S

T

T

D

P

L

L

F

Y

active site: K40 (= K46), S70 (= S74), E200 (= E214), S204 (≠ A218), S263 (≠ T279)
binding (3s)-3-hydroxybutanoic acid: K40 (= K46), G71 (= G75), T73 (= T77), Q141 (= Q155), G219 (= G235)
binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ D186), G173 (≠ V187), G175 (= G189), T176 (= T190), T179 (= T193), G219 (= G235), S263 (≠ T279), P289 (≠ C305)

2ecoA Crystal structure of t.Th. Hb8 o-acetylserine sulfhydrylase complexed with 4-methylvalerate
44% identity, 96% coverage: 12:317/318 of query aligns to 6:301/302 of 2ecoA

query
sites
2ecoA

A

A

I

I

G

G

H

K

T

T

P

P

L

V

I

V

E

R

L

L

G

A

R

K

V

V

G

V

R

E

D

P

L

D

P

M

A

A

R

E

I

V

W

W

A

V

K

K

A

L

E

E

F

G

M

L

N

N

P

P

G

G

S

S

M

I

K
|
K

D

D

R

R

I

P

A

A

L

W

K

Y

M

M

I

I

E

K

D

D

A

A

E

E

Q

E

A

R

G

G

K

I

L

L

K

R

P

P

G

G

-

S

-

G

D

Q

T

V

V

I

L

V

E

E

E

P

T
|
T

S
|
S

G
|
G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

M

M

V

I

C

A

A

A

I

S

K

R

G

G

Y

Y

P

R

F

L

I

I

A

L

V

T

M

M

S

P

E

A

G

Q

N

M

S

S

P

E

E

E

R

R

R

K

Q

R

I

V

L

L

K

K

A

A

L

F

G

G

A

A

K

E

V

L

E

V

L

L

V

T

-

D

P

P

Q

E

A

R

E

R

G

-

K

-

P

-

G

-

Q

-

V

-

T

-

G

-

D

-

L

M

A

L

L

A

V

A

E

R

K

E

R

E

A

A

G

L

E

R

L

L

Q

K

Q

E

E

E

L

L

G

G

A

A

F

F

W

M

V

P

N

D

Q
|
Q

F

F

H

K

N

N

P

P

S

A

N

N

C

V

A

R

G

A

H

H

Y

Y

E

E

T

T

A

G

Q

P

E

E

I

L

W

Y

E

E

Q

A

M

L

E

E

G

G

R

R

I

I

D

D

Y

A

F

F

V

V

D
x
Y

V

G

V

S

G
|
G

T
|
T

S

G

G

G

T
|
T

F

I

T

T

G

G

I

V

A

G

T

R

A

Y

L

L

K

K

E

E

K

R

D

I

P

P

K

H

I

V

Q

K

C

V

W

I

V

A

V

V

E
|
E

P

P

A

A

S

R

A
x
S

P

N

V

V

L

L

A

S

G

G

K

G

P

K

V

M

T

G

N

-

P

-

K

Q

H

H

V

G

L

F

Q

Q

G
|
G

S

M

S

G

Y

P

A

G

K

F

I

I

P

P

A

E

L

N

W

L

K

D

P

L

E

S

V

L

C

L

D

D

G

G

Y

V

I

I

T

Q

V

V

T

W

D

E

G

E

E

D

A

A

I

F

R

P

T

L

S

A

R

R

L

L

A

A

S

R

E

E

G

G

L

L

L

F

V

L

G

G

Y

M

T
x
S

A

S

G

G

N

I

V

V

A

W

A

A

L

L

R

Q

M

V

A

A

G

R

W

E

C

L

D

G

P

P

G

G

A

K

N

R

I

V

V

A

T

C

I

I

L

S

C
x
P

D
|
D

S

G

G

G

M

W

K

K

Y

Y

L

L

S

S

T

T

D

P

L

L

F

Y

active site: K40 (= K46), S70 (= S74), E200 (= E214), S204 (≠ A218), S263 (≠ T279)
binding 4-methyl valeric acid: K40 (= K46), T69 (= T73), G71 (= G75), T73 (= T77), Q141 (= Q155), G175 (= G189), T176 (= T190), G219 (= G235)
binding pyridoxal-5'-phosphate: K40 (= K46), N72 (= N76), Y172 (≠ D186), G175 (= G189), T176 (= T190), T179 (= T193), G219 (= G235), S263 (≠ T279), P289 (≠ C305), D290 (= D306)

2bhtA Crystal structure of o-acetylserine sulfhydrylase b (see paper)
39% identity, 98% coverage: 7:317/318 of query aligns to 2:292/294 of 2bhtA

query
sites
2bhtA

S

S

S

T

V

L

L

E

E

Q

A

T

I

I

G

G

H

N

T

T

P

P

L

L

I

V

E

K

L

L

G

Q

R

R

V

M

G

G

R

P

D

D

L

N

P

G

A

S

R

E

I

V

W

W

A

L

K

K

A

L

E

E

F

G

M

N

N

N

P

P

G

A

G

G

S

S

M

V

K
|
K

D

D

R

R

I

A

A

A

L

L

K

S

M

M

I

I

E

V

D

E

A

A

E

E

Q

K

A

R

G

G

K

R

L

I

K

K

P

P

G

G

D

D

T

V

V

L

L

I

E

E

E

A

T

T

S
|
S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

M

M

V

I

C

A

A

A

I

L

K

K

G

G

Y

Y

P

R

F

M

I

K

A

L

V

L

M

M

S

P

E

D

G

N

N

M

S

S

P

Q

E

E

R

R

Q

A

I

A

L

M

K

R

A

A

L

Y

G

G

A

A

K

E

V

L

E

I

L

L

V

V

P

T

Q

K

A

E

E

Q

G

G

G

M

K

E

P

G

G

A

Q

R

V

-

T

-

G

-

D

-

D

D

L

L

A

A

L

L

V

E

E

M

K

A

R

N

A

R

G

G

E

E

L

G

Q

K

Q

-

E

-

L

-

G

-

A

-

F

-

W

L

V

L

N

D

Q

Q

F

F

H

N

N

N

P

P

S

D

N

N

C

P

A

K

G

A

H

H

Y

Y

E

T

T

T

A

G

Q

P

E

E

I

I

W

W

E

Q

Q

Q

M

T

E

G

G

G

R

R

I

I

D

T

Y

H

F

F

V

V

D

S

V

S

V
x
M

G
|
G

T
|
T

S
x
T

G

G

T
|
T

F

I

T

T

G

G

I

V

A

S

T

E

A

F

L

M

K

R

E

E

K

Q

D

S

P

K

K

P

I

V

Q

T

C

I

W

V

V

G

V

L

E
x
Q

P

P

A

E

S

E

A
x
G

P

S

V

S

L

I

A

P

G
|
G

K

-

P

-

V

-

T

-

N

-

P

-

K

-

H

-

V

-

L

I

Q

R

G

R

S

W

S

P

Y

T

A

E

K

Y

I

L

P

P

A

G

L

I

W

F

K

N

P

A

E

S

V

L

C

V

D

D

G

E

Y

V

I

L

T

D

V

I

T

H

D

Q

G

R

E

D

A

A

I

E

R

N

T

T

S

M

R

R

R

E

L

L

A

A

S

V

E

R

E

E

G

G

L

I

L

F

V

C

G

G

Y

V

T
x
S

A

S

G

G

N

A

V

V

A

A

A

G

A

A

L

L

R

R

M

V

A

A

G

K

W

-

C

A

D

N

P

P

G

D

A

A

N

V

I

V

V

V

T

A

I

I

L

I

C
|
C

D

D

S

R

G

G

M

D

K

R

Y

Y

L

L

S

S

T

T

D

G

L

V

F

F

active site: K41 (= K46), S69 (= S74), Q199 (≠ E214), G203 (≠ A218), S255 (≠ T279), C280 (= C305)
binding pyridoxal-5'-phosphate: K41 (= K46), N71 (= N76), M173 (≠ V188), G174 (= G189), T175 (= T190), T176 (≠ S191), T178 (= T193), G208 (= G223), S255 (≠ T279), C280 (= C305)

4lmbA Crystal structure analysis of o-acetylserine sulfhydrylase cysk2 complexed with cystine from microcystis aeruginosa 7806 (see paper)
43% identity, 98% coverage: 6:318/318 of query aligns to 4:309/310 of 4lmbA

query
sites
4lmbA

C

A

S

R

S

D

V

I

L

T

E

Q

A

L

I

V

G

G

H

R

T

T

P

P

L

L

I

V

E

Q

L

L

G

N

R

R

-

I

-

P

V

V

G

A

R

E

D

G

L

V

P

K

A

A

R

R

I

I

W

V

A

V

K

K

A

L

E

E

F

S

M

M

N

N

P

P

G

A

S

S

M

V

K
|
K

D

D

R

R

I

I

A

G

L

V

K

S

M

M

I

V

E

E

D

D

A

A

E

E

Q

A

A

A

G

G

K

L

L

I

K

H

P

P

G

D

D

K

T

T

V

I

L

L

-

V

E

E

E

P

T
|
T

S
|
S

G

G

N
|
N

T
|
T

G

G

I

I

G

A

L

L

A

A

M

M

V

V

C

A

A

A

I

A

K

K

G

G

Y

Y

P

R

F

L

I

V

A

L

V

T

M

M

S

P

E

E

G

T

N
x
M

S

S

P

L

E

E

R

R

Q

A

I

M

L

L

K

K

A

A

L

Y

G

G

A

A

K

Q

V

L

E

E

L

L

V

T

P

P

Q

G

A

S

E

Q

G

G

G
x
M

K

E

P

-

G

G

Q

A

V

I

T

T

G

-

D

-

L

-

A

-

L

-

V

-

E

-

K

-

R

R

A

A

G

E

E

E

L

I

Q

V

Q

E

E

N

L

T

-

P

G

N

A

A

F

Y

W

S

V

L

N

Q

Q
|
Q

F
|
F

H

R

N

N

P

P

S

A

N

N

C

P

A

K

G

I

H

H

Y

R

E

E

T

T

A

A

Q

E

E

E

I

I

W

W

E

A

Q

D

M

T

E

D

G

G

R

L

I

V

D

D

Y

I

F

V

V

I

D

G

V

G

V
|
V

G
|
G

T
|
T

S
x
G

G

G

T
|
T

F

I

T

T

G

G

I

I

A

A

T

E

A

T

L

I

K

K

E

P

K

R

D

R

P

P

K

Q

I

F

Q

Q

C

A

W

I

V

A

V

V

E

E

P

P

A

S

S

N

A

S

P

P

V

V

L

L

A

S

G

G

K

G

P

-

V

-

T

-

N

Q

P

P

-

G

K

P

H

H

V

K

L

I

Q
|
Q

G
|
G

S
x
I

S

G

Y
x
A

A

G

K

F

I

I

P

P

A

A

L

I

W

F

K

R

P

P

E

E

V

L

C

I

D

D

G

E

Y

V

I

I

T

I

V

V

T

D

D

D

G

T

E

E

A

A

I

F

R

A

T

Y

S

A

R

R

L

L

A

A

S

R

E

Q

E

E

G

G

L

L

V

S

G

G

Y

I

T
x
S

A

A

G

G

G

A

N

A

V

L

A

W

A

A

L

I

R

Q

M

V

A

G

G

K

W

R

C

P

D

E

P

N

G

E

A

D

N

K

I

L

V

I

T

V

I

M

L

I

C

Q

D
x
P

S

S

-

F

G

G

M

E

K

R

Y

Y

L

L

S

S

T

T

D

A

L

L

F

F

K

K

active site: K46 (= K46), S269 (≠ T279)
binding cysteine: K46 (= K46), T74 (= T73), S75 (= S74), N77 (= N76), T78 (= T77), M101 (≠ N100), M125 (≠ G124), M125 (≠ G124), Q147 (= Q155), F148 (= F156), Q224 (= Q234), G225 (= G235), G225 (= G235), I226 (≠ S236), A228 (≠ Y238)
binding pyridoxal-5'-phosphate: K46 (= K46), N77 (= N76), V180 (= V188), G181 (= G189), T182 (= T190), G183 (≠ S191), T185 (= T193), G225 (= G235), S269 (≠ T279), P296 (≠ D306)

P16703 Cysteine synthase B; CSase B; O-acetylserine (thiol)-lyase B; OAS-TL B; O-acetylserine sulfhydrylase B; EC 2.5.1.47 from Escherichia coli (strain K12) (see paper)
39% identity, 98% coverage: 7:317/318 of query aligns to 2:292/303 of P16703

query
sites
P16703

S

S

S

T

V

L

L

E

E

Q

A

T

I

I

G

G

H

N

T

T

P

P

L

L

I

V

E

K

L

L

G

Q

R

R

V

M

G

G

R

P

D

D

L

N

P

G

A

S

R

E

I

V

W

W

A

L

K

K

A

L

E

E

F

G

M

N

N

N

P

P

G

A

G

G

S

S

M

V

K

K

D

D

R

R

I

A

A

A

L

L

K

S

M

M

I

I

E

V

D

E

A

A

E

E

Q

K

A

R

G

G

K

E

L

I

K

K

P

P

G

G

D

D

T

V

V

L

L

I

E

E

E

A

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

M

M

V

I

C

A

A

A

I

L

K

K

G

G

Y

Y

P

R

F

M

I

K

A

L

V

L

M

M

S

P

E

D

G

N

N

M

S

S

P

Q

E

E

R

R

Q

A

I

A

L

M

K

R

A

A

L

Y

G

G

A

A

K

E

V

L

E

I

L

L

V

V

P

T

Q

K

A

E

E

Q

G

G

G

M

K

E

P

G

G

A

Q

R

V

-

T

-

G

-

D

-

D

D

L

L

A

A

L

L

V

E

E

M

K

A

R

N

A

R

G

G

E

E

L

G

Q

K

Q

-

E

-

L

-

G

-

A

-

F

-

W

L

V

L

N

D

Q

Q

F

F

H

N

N

N

P

P

S

D

N

N

C

P

A

Y

G

A

H

H

Y

Y

E

T

T

T

A

G

Q

P

E

E

I

I

W

W

E

Q

Q

Q

M

T

E

G

G

G

R

R

I

I

D

T

Y

H

F

F

V

V

D

S

V

S

V

M

G

G

T

T

S

T

G

G

T

T

F

I

T

T

G

G

I

V

A

S

T

R

A

F

L

M

K

R

E

E

K

Q

D

S

P

K

K

P

I

V

Q

T

C

I

W

V

V

G

V

L

E

Q

P

P

A

E

S

E

A

G

P

S

V

S

L

I

A

P

G

G

K

-

P

-

V

-

T

-

N

-

P

-

K

-

H

-

V

-

L

I

Q

R

G

R

S

W

S

P

Y

T

A

E

K

Y

I

L

P

P

A

G

L

I

W

F

K

N

P

A

E

S

V

L

C

V

D

D

G

E

Y

V

I

L

T

D

V

I

T

H

D

Q

G

R

E

D

A

A

I

E

R

N

T

T

S

M

R

R

R

E

L

L

A

A

S

V

E

R

E

E

G

G

L

I

L

F

V

C

G

G

Y

V

T
x
S

A

S

G

G

N

A

V

V

A

A

A

G

A

A

L

L

R

R

M

V

A

A

G

K

W

-

C

A

D

N

P

P

G

D

A

A

N

V

I

V

V

V

T

A

I

I

L

I

C

C

D

D

S

R

G

G

M

D

K

R

Y

Y

L

L

S

S

T

T

D

G

L

V

F

F

N71 (= N76) binding pyridoxal 5'-phosphate
S255 (≠ T279) binding pyridoxal 5'-phosphate

4lmaA Crystal structure analysis of o-acetylserine sulfhydrylase cysk1 from microcystis aeruginosa 7806 (see paper)
44% identity, 97% coverage: 9:318/318 of query aligns to 7:309/318 of 4lmaA

query
sites
4lmaA

V

V

L

T

E

E

A

L

I

V

G

G

H

R

T

T

P

P

L

L

I

V

E

Q

L

L

G

N

R

R

V

I

-

P

-

Q

G

A

R

E

D

G

L

C

P

L

A

G

R

R

I

I

W

V

A

M

K

K

A

L

E

E

F

G

M

M

N

N

P

P

G

A

S

S

M

V

K
|
K

D

D

R

R

I

I

A

G

L

T

K

H

M

M

I

I

E

N

D

S

A

A

E

E

Q

K

A

A

G

G

K

L

L

I

K

N

P

P

G

E

D

T

T

T

V

V

L

L

-

V

E

E

E

P

T

T

S

S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

M

M

V

T

C

A

A

A

I

A

K

K

G

G

Y

Y

P

R

F

L

I

I

A

L

V

T

M

M

S

P

E

E

G

T

N

M

S

S

P

L

E

E

R

R

Q

A

I

M

L

L

K

K

A

A

L

Y

G

G

A

A

K

T

V

L

E

E

L

L

V

T

P

P

Q

G

A

S

E

Q

G

G

G

M

K

K

P

-

G

G

Q

A

V

I

T

L

G

-

D

-

L

-

A

-

L

-

V

-

E

-

K

-

R

R

A

A

G

Q

E

Q

L

I

Q

V

Q

D

E

S

L

I

-

P

G

G

A

A

F

Y

W

M

V

L

N

Q

Q

Q

F

F

H

R

N

N

P

P

S

S

N

N

C

P

A

E

G

I

H

H

Y

R

E

L

T

T

A

A

Q

E

E

E

I

I

W

W

E

Q

Q

D

M

T

E

E

G

G

R

Q

I

V

D

D

Y

F

F

I

V

V

D

A

V

G

V

V

G
|
G

T
|
T

S
x
G

G

G

T
|
T

F

I

T

T

G

G

I

V

A

A

T

E

A

V

L

I

K

K

E

S

K

R

D

K

P

P

K

S

I

F

Q

Q

C

V

W

V

V

A

V

V

E

E

P

P

A

F

S

N

A

S

P

P

V

V

L

I

A

S

G

G

K

G

P

-

V

-

T

-

N

N

P

P

-

G

K

P

H

H

V

K

L

I

Q

Q

G
|
G

S

I

S

G

Y

A

A

G

K

F

I

I

P

P

A

E

L

V

W

L

K

R

P

T

E

D

V

L

C

I

D

D

G

E

Y

V

I

I

T

T

V

V

T

S

D

D

G

E

E

E

A

A

I

F

R

Q

T

F

S

G

R

R

L

L

A

A

S

K

E

E

G

G

L

L

V

S

G

G

Y

I

T
x
S

A

S

G

G

G

A

N

N

V

L

A

C

A

A

L

I

R

Q

M

L

A

A

G

Q

W

R

C

P

-

E

D

N

P

E

G

G

A

K

N

L

I

I

V

V

T

V

I

I

L

Q

C
x
P

D

S

S

F

G

G

M

E

K

R

Y

Y

L

L

S

S

T

T

D

L

L

M

F

F

K

Q

active site: K46 (= K46), S269 (≠ T279)
binding pyridoxal-5'-phosphate: K46 (= K46), N77 (= N76), G181 (= G189), T182 (= T190), G183 (≠ S191), T185 (= T193), G225 (= G235), S269 (≠ T279), P296 (≠ C305)

3zeiA Structure of the mycobacterium tuberculosis o-acetylserine sulfhydrylase (oass) cysk1 in complex with a small molecule inhibitor (see paper)
43% identity, 97% coverage: 6:312/318 of query aligns to 4:300/300 of 3zeiA

query
sites
3zeiA

C

A

S

E

S

D

V

I

L

T

E

Q

A

L

I

I

G

G

H

R

T

T

P

P

L

L

I

V

E

R

L

L

G

R

R

R

V

V

G

T

R

D

D

G

L

A

P

V

A

A

R

D

I

I

W

V

A

A

K

K

A

L

E

E

F

F

M

F

N

N

P

P

G

A

G

N

S

S

M

V

K
|
K

D

D

R

R

I

I

A

G

L

V

K

A

M

M

I

L

E

Q

D

A

A

A

E

E

Q

Q

A

A

G

G

K

L

L

I

K

K

P

P

G

D

D

T

T

I

V

I

L

L

E

E

E

P

T
|
T

S
|
S

G

G

N
|
N

T

T

G

G

I

I

G

A

L

L

A

A

M

M

V

V

C

C

A

A

I

A

K

R

G

G

Y

Y

P

R

F

C

I

V

A

L

V

T

M

M

S

P

E

E

G

T

N

M

S

S

P

L

E

E

R

R

Q

M

I

L

L

L

K

R

A

A

L

Y

G

G

A

A

K

E

V

L

E

I

L

L

V

T

P

P

Q

G

A

A

E

D

G

G

G

M

K

S

P

G

G

A

Q
x
I

V

A

T

K

G

A

D

E

L

L

A

A

L

K

V

T

E

D

K

Q

R

R

A

-

G

-

E

-

L

-

Q

-

E

-

L

-

G

-

A

Y

F

F

W

V

V

P

N

Q

Q
|
Q

F
|
F

H

E

N

N

P

P

S

A

N

N

C

P

A

A

G

I

H

H

Y

R

E

V

T

T

A

A

Q

E

E

E

I

V

W

W

E

R

Q

D

M

T

E

D

G

G

R

K

I

V

D

D

Y

I

F

V

V

V

D

A

V

G

V
|
V

G
|
G

T
|
T

S
x
G

G

G

T
|
T

F

I

T

T

G

G

I

V

A

A

T

Q

A

V

L

I

K

K

E

E

K

R

D

K

P

P

K

S

I

A

Q

R

C

F

W

V

V

A

V

V

E

E

P

P

A

A

S

A

A

S

P

P

V

V

L

L

A

S

G

G

K

G

P

-

V

-

T

Q

N
x
K

P

G

K

P

H

H

V

P

L

I

Q

Q

G
|
G

S

I

S

G

Y
x
A

A

G

K
x
F

I

V

P

P

A

P

L

V

W

L

K

D

P

Q

E

D

V

L

C

V

D

D

G

E

Y

I

I

I

T

T

V

V

T

G

D

N

G

E

E

D

A

A

I

L

R

N

T

V

S

A

R

R

L

L

A

A

S

R

E

E

G

G

L

L

V

V

G

G

Y

I

T
x
S

A

S

G

G

G

A

N

A

V

T

A

V

A

A

L

L

R

Q

M

V

A

A

G

R

W

R

C

P

-

E

D

N

P

A

G

G

A

K

N

L

I

I

V

V

T

V

I

V

L

L

C
x
P

D
|
D

S

F

G

G

M

E

K

R

Y

Y

L

L

active site: K44 (= K46), S266 (≠ T279), P293 (≠ C305)
binding 3-[(Z)-[(5Z)-5-[[2-(2-hydroxy-2-oxoethyloxy)phenyl]methylidene]-3-methyl-4-oxidanylidene-1,3-thiazolidin-2-ylidene]amino]benzoic acid: T71 (= T73), S72 (= S74), I126 (≠ Q128), Q144 (= Q155), F145 (= F156), K215 (≠ N228), G222 (= G235), A225 (≠ Y238), F227 (≠ K240)
binding pyridoxal-5'-phosphate: K44 (= K46), N74 (= N76), V177 (= V188), G178 (= G189), T179 (= T190), G180 (≠ S191), T182 (= T193), G222 (= G235), S266 (≠ T279), P293 (≠ C305), D294 (= D306)

2q3cA 2.1 a resolution crystal structure of o-acetylserine sulfhydrylase (oass) holoenzyme from mycobacterium tuberculosis in complex with the inhibitory peptide dfsi (see paper)
43% identity, 97% coverage: 6:312/318 of query aligns to 4:300/300 of 2q3cA

query
sites
2q3cA

C

A

S

E

S

D

V

I

L

T

E

Q

A

L

I

I

G

G

H

R

T

T

P

P

L

L

I

V

E

R

L

L

G

R

R

R

V

V

G

T

R

D

D

G

L

A

P

V

A

A

R

D

I

I

W

V

A

A

K

K

A

L

E

E

F

F

M

F

N

N

P

P

G

A

G

N

S

S

M

V

K
|
K

D

D

R

R

I

I

A

G

L

V

K

A

M

M

I

L

E

Q

D

A

A

A

E

E

Q

Q

A

A

G

G

K

L

L

I

K

K

P

P

G

D

D

T

T

I

V

I

L

L

E

E

E

P

T
|
T

S
|
S

G
|
G

N

N

T
|
T

G

G

I

I

G

A

L

L

A

A

M

M

V

V

C

C

A

A

I

A

K

R

G

G

Y

Y

P

R

F

C

I

V

A

L

V

T

M

M

S

P

E

E

G

T

N

M

S

S

P

L

E

E

R

R

Q

M

I

L

L

L

K

R

A

A

L

Y

G

G

A

A

K

E

V

L

E

I

L

L

V

T

P

P

Q

G

A

A

E

D

G

G

G
x
M

K

S

P

G

G

A

Q

I

V

A

T

K

G

A

D

E

L

L

A

A

L

K

V

T

E

D

K

Q

R

R

A

-

G

-

E

-

L

-

Q

-

E

-

L

-

G

-

A

Y

F

F

W

V

V

P

N

Q

Q
|
Q

F

F

H

E

N

N

P

P

S

A

N

N

C

P

A

A

G

I

H

H

Y

R

E

V

T

T

A

A

Q

E

E

E

I

V

W

W

E

R

Q

D

M

T

E

D

G

G

R

K

I

V

D

D

Y

I

F

V

V

V

D

A

V

G

V

V

G

G

T

T

S

G

G

G

T

T

F

I

T

T

G

G

I

V

A

A

T

Q

A

V

L

I

K

K

E

E

K

R

D

K

P

P

K

S

I

A

Q

R

C

F

W

V

V

A

V

V

E

E

P

P

A

A

S

A

A

S

P

P

V

V

L

L

A

S

G

G

K

G

P

-

V

-

T

Q

N
x
K

P

G

K

P

H

H

V

P

L

I

Q

Q

G
|
G

S

I

S

G

Y
x
A

A

G

K

F

I

V

P

P

A

P

L

V

W

L

K

D

P

Q

E

D

V

L

C

V

D

D

G

E

Y

I

I

I

T

T

V

V

T

G

D

N

G

E

E

D

A

A

I

L

R

N

T

V

S

A

R

R

L

L

A

A

S

R

E

E

G

G

L

L

V

V

G

G

Y

I

T
x
S

A

S

G

G

G

A

N

A

V

T

A

V

A

A

L

L

R

Q

M

V

A

A

G

R

W

R

C

P

-

E

D

N

P

A

G

G

A

K

N

L

I

I

V

V

T

V

I

V

L

L

C
x
P

D

D

S

F

G

G

M

E

K

R

Y

Y

L

L

active site: K44 (= K46), S266 (≠ T279), P293 (≠ C305)
binding : T71 (= T73), S72 (= S74), G73 (= G75), T75 (= T77), M122 (≠ G124), Q144 (= Q155), K215 (≠ N228), G222 (= G235), A225 (≠ Y238)

4pcuA Crystal structure of delta516-525 e201s human cystathionine beta- synthase with adomet (see paper)
40% identity, 99% coverage: 2:316/318 of query aligns to 31:342/486 of 4pcuA

query
sites
4pcuA

S

S

P

P

I

K

K

I

C

L

S

P

S

D

V

I

L

L

E

K

A

K

I

I

G

G

H

D

T

T

P

P

L

M

I

V

E

R

L

I

G

N

R

K

V

I

G

G

R

K

D

K

-

F

-

G

L

L

P

K

A

C

R

E

I

L

W

L

A

A

K

K

A

C

E

E

F

F

M

F

N

N

P

A

G

G

S

S

M

V

K
|
K

D

D

R

R

I

I

A

S

L

L

K

R

M

M

I

I

E

E

D

D

A

A

E

E

Q

R

A

D

G

G

K

T

L

L

K

K

P

P

G

G

D

D

T

T

V

I

L

I

E

E

E

P

T

T

S
|
S

G

G

N
|
N

T

T

G

G

I

I

G

G

L

L

A

A

M

L

V

A

C

A

A

A

I

V

K

R

G

G

Y

Y

P

R

F

C

I

I

A

I

V

V

M

M

S

P

E

E

G

K

N

M

S

S

P

S

E

E

R

K

R

V

Q

D

I

V

L

L

K

R

A

A

L

L

G

G

A

A

K

E

V

I

E

V

L

R

V

T

P

P

Q

-

A

A

E

R

G

F

G

D

K

S

P

P

G

S

Q

S

V

H

T

V

G

G

D

-

L

-

A

-

L

-

V

-

E

-

K

-

R

V

A

A

G

W

E

R

L

L

Q

K

Q

N

E

E

L

I

-

P

G

N

A

S

F

H

W

I

V

L

N

D

Q

Q

F

Y

H

R

N

N

P
x
A

S

S

N

N

C
x
P

A
x
L

G

A

H

H

Y
|
Y

E

D

T

T

A

A

Q

D

E

E

I

I

W

L

E

Q

Q

Q

M

C

E

D

G

G

R

K

I

L

D

D

Y

M

F

L

V

V

D

A

V

S

V

V

G
|
G

T
|
T

S
x
G

G

G

T
|
T

F

I

T

T

G

G

I

I

A

A

T
x
R

A

K

L

L

K

K

E

E

K

K

D

C

P

P

K

G

I

C

Q

R

C

I

W

I

V

G

V

V

E
x
D

P

P

A

E

S

G

A

S

P

I

V

L

L

A

A

E

G

P

K

E

P

E

V

L

T

N

N

Q

P

T

K

E

H

Q

V

T

-

T

-

Y

-

E

L

V

Q

E

G
|
G

S

I

S

G

Y

Y

A

D

K

F

I

I

P

P

A
x
T

L

V

W

L

K

D

P

R

E

T

V

V

C

V

D

D

G

K

Y

W

I

F

T

K

V

S

T

N

D

D

G

E

E

E

A

A

I

F

R

T

T

F

S

A

R

R

R

M

L

L

A

I

S

A

E

Q

E

E

G

G

L

L

V

C

G

G

Y

G

T
x
S

A

A

G

G

G

S

N

T

V

V

A

A

A

V

A

A

L

V

R

K

M

A

A

A

G

Q

W

E

C

L

D

Q

P

E

G

G

A

Q

N

R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

S

S

G

V

M

R

K

N

Y

Y

L

M

S

T

T

K

D

F

L

L

active site: K77 (= K46), S105 (= S74), D237 (≠ E214), S305 (≠ T279)
binding protoporphyrin ix containing fe: A182 (≠ P159), P185 (≠ C162), L186 (≠ A163), Y189 (= Y166), R222 (≠ T199), T269 (≠ A243)
binding pyridoxal-5'-phosphate: K77 (= K46), N107 (= N76), G212 (= G189), T213 (= T190), G214 (≠ S191), T216 (= T193), G261 (= G235), S305 (≠ T279), P331 (≠ C305), D332 (= D306)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 8, 9, 10, 11, 12, 20, 21, 22, 23
binding s-adenosylmethionine: 376, 396, 397, 398, 399, 476, 478, 479

8s5hA Full-length human cystathionine beta-synthase with c-terminal 6xhis- tag, basal state, helical reconstruction (see paper)
40% identity, 99% coverage: 2:316/318 of query aligns to 32:345/507 of 8s5hA

query
sites
8s5hA

S

S

P

P

I

K

K

I

C

L

S

P

S

D

V

I

L

L

E

K

A

K

I

I

G

G

H

D

T

T

P

P

L

M

I

V

E

R

L

I

G

N

R

K

V

I

G

G

R

K

D

K

-

F

-

G

L

L

P

K

A

C

R

E

I

L

W

L

A

A

K

K

A

C

E

E

F

F

M

F

N

N

P

A

G

G

S

S

M

V

K

K

D

D

R

R

I

I

A

S

L

L

K

R

M

M

I

I

E

E

D

D

A

A

E

E

Q

R

A

D

G

G

K

T

L

L

K

K

P

P

G

G

D

D

T

T

V

I

L

I

E

E

E

P

T

T

S

S

G

G

N

N

T

T

G

G

I

I

G

G

L

L

A

A

M

L

V

A

C

A

A

A

I

V

K

R

G

G

Y

Y

P

R

F

C

I

I

A

I

V

V

M

M

S

P

E

E

G

K

N

M

S

S

P

S

E

E

R

K

R

V

Q

D

I

V

L

L

K

R

A

A

L

L

G

G

A

A

K

E

V

I

E

V

L

R

V

T

P

P

-

T

Q

N

A

A

E

R

G

F

G

D

K

S

P

P

G

E

Q

S

V

H

T

V

G

G

D

-

L

-

A

-

L

-

V

-

E

-

K

-

R

V

A

A

G

W

E

R

L

L

Q

K

Q

N

E

E

L

I

-

P

G

N

A

S

F

H

W

I

V

L

N

D

Q

Q

F

Y

H

R

N

N

P
x
A

S

S

N

N

C

P

A

L

G

A

H

H

Y
|
Y

E

D

T

T

A

A

Q

D

E

E

I

I

W

L

E

Q

Q

Q

M

C

E

D

G

G

R

K

I

L

D

D

Y

M

F

L

V

V

D

A

V

S

V

V

G

G

T

T

S

G

G

G

T

T

F

I

T

T

G

G

I

I

A

A

T
x
R

A

K

L

L

K

K

E

E

K

K

D

C

P

P

K

G

I

C

Q

R

C

I

W

I

V

G

V

V

E

D

P

P

A

E

S

G

A

S

P

I

V

L

L

A

A

E

G

P

K

E

P

E

V

L

T

N

N

Q

P

T

K

E

H

Q

V

T

-

T

-

Y

-

E

L

V

Q

E

G

G

S

I

S

G

Y

Y

A

D

K

F

I

I

P

P

A

T

L

V

W

L

K

D

P

R

E

T

V

V

C

V

D

D

G

K

Y

W

I

F

T

K

V

S

T

N

D

D

G

E

E

E

A

A

I

F

R

T

T

F

S

A

R

R

R

M

L

L

A

I

S

A

E

Q

E

E

G

G

L

L

V

C

G

G

Y

G

T

S

A

A

G

G

G

S

N

T

V

V

A

A

A

V

A

A

L

V

R

K

M

A

A

A

G

Q

W

E

C

L

D

Q

P

E

G

G

A

Q

N

R

I

C

V

V

T

V

I

I

L

L

C

P

D

D

S

S

G

V

M

R

K

N

Y

Y

L

M

S

T

T

K

D

F

L

L

binding protoporphyrin ix containing fe: A185 (≠ P159), Y192 (= Y166), R225 (≠ T199)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 10, 11, 17, 22, 23, 24

7qgtB Crystal structure of human cystathionine beta-synthase (delta516-525) in complex with aoaa. (see paper)
40% identity, 99% coverage: 2:316/318 of query aligns to 33:346/500 of 7qgtB

query
sites
7qgtB

S

S

P

P

I

K

K

I

C

L

S

P

S

D

V

I

L

L

E

K

A

K

I

I

G

G

H

D

T

T

P

P

L

M

I

V

E

R

L

I

G

N

R

K

V

I

G

G

R

K

D

K

-

F

-

G

L

L

P

K

A

C

R

E

I

L

W

L

A

A

K

K

A

C

E

E

F

F

M

F

N

N

P

A

G

G

S

S

M

V

K
|
K

D

D

R

R

I

I

A

S

L

L

K

R

M

M

I

I

E

E

D

D

A

A

E

E

Q

R

A

D

G

G

K

T

L

L

K

K

P

P

G

G

D

D

T

T

V

I

L

I

E

E

E

P

T
|
T

S
|
S

G

G

N
|
N

T
|
T

G

G

I

I

G

G

L

L

A

A

M

L

V

A

C

A

A

A

I

V

K

R

G

G

Y

Y

P

R

F

C

I

I

A

I

V

V

M

M

S

P

E

E

G

K

N

M

S

S

P

S

E

E

R

K

R

V

Q

D

I

V

L

L

K

R

A

A

L

L

G

G

A

A

K

E

V

I

E

V

L

R

V

T

P

P

-

T

Q

N

A

A

E

R

G

F

G

D

K

S

P

P

G

E

Q

S

V

H

T

V

G

G

D

-

L

-

A

-

L

-

V

-

E

-

K

-

R

V

A

A

G

W

E

R

L

L

Q

K

Q

N

E

E

L

I

-

P

G

N

A

S

F

H

W

I

V

L

N

D

Q
|
Q

F

Y

H

R

N

N

P
x
A

S

S

N

N

C
x
P

A
x
L

G

A

H

H

Y
|
Y

E

D

T

T

A

A

Q

D

E

E

I

I

W

L

E

Q

Q

Q

M

C

E

D

G

G

R

K

I

L

D

D

Y

M

F

L

V

V

D

A

V

S

V

V

G
|
G

T
|
T

S
x
G

G

G

T
|
T

F

I

T

T

G

G

I

I

A

A

T
x
R

A

K

L

L

K

K

E

E

K

K

D

C

P

P

K

G

I

C

Q

R

C

I

W

I

V

G

V

V

E

D

P

P

A

E

S

G

A

S

P

I

V

L

L

A

A

E

G

P

K

E

P

E

V

L

T

N

N

Q

P

T

K

E

H

Q

V

T

-

T

-

Y

-

E

L

V

Q

E

G
|
G

S

I

S

G

Y

Y

A

D

K

F

I

I

P

P

A

T

L

V

W

L

K

D

P

R

E

T

V

V

C

V

D

D

G

K

Y

W

I

F

T

K

V

S

T

N

D

D

G

E

E

E

A

A

I

F

R

T

T

F

S

A

R

R

R

M

L

L

A

I

S

A

E

Q

E

E

G

G

L

L

V

C

G

G

Y

G

T
x
S

A

A

G

G

G

S

N

T

V

V

A

A

A

V

A

A

L

V

R

K

M

A

A

A

G

Q

W

E

C

L

D

Q

P

E

G

G

A

Q

N

R

I

C

V

V

T

V

I

I

L

L

C
x
P

D
|
D

S

S

G

V

M

R

K

N

Y

Y

L

M

S

T

T

K

D

F

L

L

binding protoporphyrin ix containing fe: A186 (≠ P159), P189 (≠ C162), L190 (≠ A163), Y193 (= Y166), R226 (≠ T199)
binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: K79 (= K46), T106 (= T73), S107 (= S74), N109 (= N76), T110 (= T77), Q182 (= Q155), G216 (= G189), T217 (= T190), G218 (≠ S191), T220 (= T193), G265 (= G235), S309 (≠ T279), P335 (≠ C305), D336 (= D306)

Sites not aligning to the query:

binding protoporphyrin ix containing fe: 10, 11, 12, 13, 14, 23, 24, 25

P35520 Cystathionine beta-synthase; Beta-thionase; Serine sulfhydrase; EC 4.2.1.22 from Homo sapiens (Human) (see 40 papers)
40% identity, 99% coverage: 2:316/318 of query aligns to 73:386/551 of P35520

query
sites
P35520

S

S

P

P

I

K

K

I

C

L

S
x
P

S

D

V

I

L

L

E

K

A

K

I

I

G
|
G

H

D

T
|
T

P

P

L

M

I

V

E

R

L

I

G

N

R

K

V

I

G

G

R

K

D

K

-

F

-

G

L
|
L

P
x
K

A

C

R

E

I

L

W

L

A

A

K

K

A
x
C

E

E

F

F

M

F

N

N

P
x
A

G

G

S

S

M

V

K
|
K

D

D

R

R

I

I

A

S

L

L

K
x
R

M
|
M

I

I

E

E

D

D

A

A

E
|
E

Q

R

A

D

G

G

K

T

L

L

K

K

P

P

G
|
G

D

D

T

T

V

I

L
x
I

E
|
E

E

P

T

T

S

S

G
|
G

N
|
N

T

T

G

G

I

I

G

G

L
|
L

A
|
A

M

L

V

A

C

A

A

A

I

V

K

R

G

G

Y

Y

P

R

F
x
C

I

I

A

I

V

V

M

M

S

P

E

E

G

K

N
x
M

S

S

P

S

E
|
E

R

K

R

V

Q

D

I
x
V

L

L

K

R

A

A

L

L

G

G

A

A

K

E

V

I

E

V

L

R

V
x
T

P

P

-

T

Q

N

A

A

E

R

G

F

G

D

K

S

P

P

G

E

Q

S

V

H

T

V

G

G

D

-

L

-

A

-

L

-

V

-

E

-

K

-

R

V

A

A

G

W

E

R

L

L

Q
x
K

Q

N

E

E

L

I

-

P

G

N

A

S

F

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P78 (≠ S7) to R: in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204608
G85 (= G14) to R: in CBSD; loss of cystathionine beta-synthase activity; dbSNP:rs863223435
T87 (= T16) to N: in CBSD; decreased cystathionine beta-synthase activity; increased aggregation
L101 (= L28) to P: in CBSD; common mutation in Irish population; loss of activity; dbSNP:rs786204757
K102 (≠ P29) to N: in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs786204609; to Q: in dbSNP:rs34040148
C109 (≠ A36) to R: in CBSD; loss of activity; dbSNP:rs778220779
A114 (≠ P41) to V: in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs121964964
K119 (= K46) modified: N6-(pyridoxal phosphate)lysine
R125 (≠ K52) to Q: in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs781444670; to W: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs886057100
M126 (= M53) to V: in CBSD; loss of activity
E131 (= E58) to D: in CBSD; linked with Q-125; loss of activity; dbSNP:rs1555875351
G139 (= G66) to R: in CBSD; mild form; dbSNP:rs121964965
I143 (≠ L70) to M: in CBSD; 4% of activity; stable; dbSNP:rs370167302
E144 (= E71) to K: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964966
G148 (= G75) to R: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs755952006
N149 (= N76) binding pyridoxal 5'-phosphate
L154 (= L81) to Q: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
A155 (= A82) to T: in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs1429138569; to V: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity
C165 (≠ F92) to Y: in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation; dbSNP:rs1347651454
M173 (≠ N100) to V: in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; natural variant: Missing (in CBSD; loss of activity)
E176 (= E103) to K: in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates; dbSNP:rs762065361
V180 (≠ I107) to A: in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation; dbSNP:rs1555875010
T191 (≠ V118) to M: in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure; dbSNP:rs121964973
K211 (≠ Q145) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
A226 (≠ P159) to T: in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure; dbSNP:rs763835246
N228 (= N161) to K: in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs1464223176; to S: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1555874803
A231 (≠ G164) to P: in CBSD; has significantly decreased levels of enzyme activity
D234 (≠ E167) to N: in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation; dbSNP:rs773734233; natural variant: Missing (in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity)
GTGGT 256:260 (≠ GTSGT 189:193) binding pyridoxal 5'-phosphate
T257 (= T190) to M: in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs758236584
T262 (= T195) to M: in CBSD; moderate form; dbSNP:rs149119723; to R: in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation
R266 (≠ T199) to K: in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability; dbSNP:rs121964969
K269 (= K202) natural variant: Missing (in CBSD; loss of expression)
C272 (≠ D205) mutation to A: Reduced heme content and cystathionine beta-synthase activity.
C275 (≠ I208) to Y: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; mutation to S: Reduced heme content and cystathionine beta-synthase activity.
I278 (≠ W211) to S: in CBSD; loss of activity; to T: in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates; dbSNP:rs5742905
D281 (≠ E214) to N: in CBSD; loss of activity
A288 (≠ L221) to T: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs141502207
E302 (vs. gap) to K: in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation; dbSNP:rs779270933
G305 (= G235) to R: in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation
G307 (≠ S237) to S: in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation; dbSNP:rs121964962
V320 (≠ C250) to A: in CBSD; has 36% of wild-type enzyme activity; dbSNP:rs781567152
D321 (= D251) to V: in CBSD; loss of activity
R336 (= R266) to C: in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure; dbSNP:rs398123151; to H: in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure; dbSNP:rs760417941
L338 (= L268) to P: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
G347 (= G277) to S: in CBSD; protein expression is comparable to wild-type; loss of activity; dbSNP:rs771298943
S349 (≠ T279) binding pyridoxal 5'-phosphate; to N: in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
T353 (≠ N283) to M: in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity; dbSNP:rs121964972
R369 (≠ N299) to C: in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; dbSNP:rs117687681
D376 (= D306) to N: in CBSD; has significantly decreased levels of enzyme activity; dbSNP:rs1170128038
R379 (≠ M309) to Q: in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure; dbSNP:rs763036586
K384 (≠ T314) to E: in CBSD; severe form; dbSNP:rs121964967

Sites not aligning to the query:

18 R → C: results in 1/3 to 2/3 the enzyme activity of the wild-type; dbSNP:rs201827340
49 P → L: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs148865119
52 binding axial binding residue
58 R → W: in CBSD; linked with V-114; 18% of activity; dbSNP:rs555959266
65 binding axial binding residue; H → R: in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs1191141364
69 A → P: in dbSNP:rs17849313
422 P → L: in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation; dbSNP:rs28934892
427 P → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs863223434
435 I → T: in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation
439 R → Q: in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation; dbSNP:rs756467921
444 D → N: in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation; dbSNP:rs28934891
449 V → G: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
456 L → P: in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure
466 S → L: in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation; dbSNP:rs121964971
500 S → L: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; dbSNP:rs755106884
526 Q → K: in CBSD; has significantly decreased levels of enzyme activity
539 L → S: in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation; dbSNP:rs121964968
540 L → Q: in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet
548 R → Q: presents 60% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure; dbSNP:rs150828989

3x43A Crystal structure of o-ureido-l-serine synthase (see paper)
42% identity, 98% coverage: 7:317/318 of query aligns to 4:302/316 of 3x43A

query
sites
3x43A

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active site: K42 (= K46), S264 (≠ T279)
binding pyridoxal-5'-phosphate: K42 (= K46), N72 (= N76), F175 (≠ V188), G176 (= G189), T177 (= T190), T178 (≠ S191), T180 (= T193), G220 (= G235), S264 (≠ T279), P290 (≠ C305), D291 (= D306)

D2Z027 O-ureido-L-serine synthase; Cysteine synthase homolog DscD; O-acetylserine sulfhydrylase; EC 2.6.99.3; EC 2.5.1.47 from Streptomyces lavendulae (see paper)
42% identity, 98% coverage: 7:317/318 of query aligns to 5:303/324 of D2Z027

query
sites
D2Z027

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F

K43 (= K46) modified: N6-(pyridoxal phosphate)lysine; mutation to A: Loss of catalytic activity, no longer binds N6-(pyridoxal phosphate)lysine.
V74 (≠ T77) mutation to T: KM for OAS is 61 mM, KM for H(2)S is unchanged.
Y97 (≠ N100) mutation to F: KM for OAS is unchanged, KM for H(2)S is 0.073 mM.; mutation to M: KM for OAS is 330 mM, KM for H(2)S is 0.084.
S121 (≠ G124) mutation to A: KM for OAS is 140 mM, KM for H(2)S is 0.095 mM.; mutation to M: KM for OAS is 44 mM, KM for H(2)S is 0.20 mM.

Query Sequence

>WP_013842638.1 NCBI__GCF_000215085.1:WP_013842638.1
MSPIKCSSVLEAIGHTPLIELGRVGRDLPARIWAKAEFMNPGGSMKDRIALKMIEDAEQA
GKLKPGDTVLEETSGNTGIGLAMVCAIKGYPFIAVMSEGNSPERRQILKALGAKVELVPQ
AEGGKPGQVTGDDLALVEKRAGELQQELGAFWVNQFHNPSNCAGHYETTAQEIWEQMEGR
IDYFVDVVGTSGTFTGIATALKEKDPKIQCWVVEPASAPVLAGKPVTNPKHVLQGSSYAK
IPALWKPEVCDGYITVTDGEAIRTSRRLASEEGLLVGYTAGGNVAAALRMAGWCDPGANI
VTILCDSGMKYLSTDLFK

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory